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Journals / Turkish Journal of Veterinary and Animal Sciences / 2015 / Cilt: 39 - Sayı: 3

The assembly of virus-like particles of porcine transmissible gastroenteritisvirus in vitro by baculovirus expression system

SONG ZHENHUI
HAIBO FENG
ZHI ZHU
XIANJIN DAI
YUE ZHOU
YUNTIAN LI
XINZHI CAO
Pages
302
Publication Date
2015-08-13
DOI
—
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

This study provides a theoretical foundation for further study on the role of TGEV structural proteins in the assembly process of virions.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Virus-like particles (VLPs) produced by recombinant expression of the major viral structural proteins could be an attractive method for transmissible gastroenteritis virus (TGEV) assembly and release.
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Key Findings & Data:Those recombinant donor plasmids were transformed into E.coli DH10Bac respectively.
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Conclusion & Impact:This study provides a theoretical foundation for further study on the role of TGEV structural proteins in the assembly process of virions.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Transmissible gastroenteritis virus · virus-like particles · baculovirus expression system

Abstract

Virus-like particles (VLPs) produced by recombinant expression of the major viral structural proteins could be an attractive method for transmissible gastroenteritis virus (TGEV) assembly and release. In this study, the M gene, sM gene, and N gene of TGEV were inserted into donor plasmid pFastBac Dual. Those recombinant donor plasmids were transformed into E.coli DH10Bac respectively. Recombinant baculoviruses were obtained by transfection of the Sf9 cells with Bacmid-M, Bacmid-sM, and Bacmid-N. The results of indirect immunofluorescence assay showed that recombinant M protein, sM protein, and N protein were expressed successfully. In vitro experiments of VLP assembly of TGEV were performed by infection of insect cells with various combinations of recombinant baculoviruses identified. It is shown that expression of M protein alone, coexpression of M plus sM protein, and coexpression of M plus N protein in Sf9 insect cells infected by recombinant baculovirus could result in the occurrence of a virion morphologically similar to TGEV. However, the sM and N protein could not generate a structure similar to the virion of TGEV when expressed alone. This study provides a theoretical foundation for further study on the role of TGEV structural proteins in the assembly process of virions.

Özet

Virus-like particles (VLPs) produced by recombinant expression of the major viral structural proteins could be an attractive method for transmissible gastroenteritis virus (TGEV) assembly and release. In this study, the M gene, sM gene, and N gene of TGEV were inserted into donor plasmid pFastBac Dual. Those recombinant donor plasmids were transformed into E.coli DH10Bac respectively. Recombinant baculoviruses were obtained by transfection of the Sf9 cells with Bacmid-M, Bacmid-sM, and Bacmid-N. The results of indirect immunofluorescence assay showed that recombinant M protein, sM protein, and N protein were expressed successfully. In vitro experiments of VLP assembly of TGEV were performed by infection of insect cells with various combinations of recombinant baculoviruses identified. It is shown that expression of M protein alone, coexpression of M plus sM protein, and coexpression of M plus N protein in Sf9 insect cells infected by recombinant baculovirus could result in the occurrence of a virion morphologically similar to TGEV. However, the sM and N protein could not generate a structure similar to the virion of TGEV when expressed alone. This study provides a theoretical foundation for further study on the role of TGEV structural proteins in the assembly process of virions.

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Cite This Article

ZHENHUI, S., FENG, H., ZHU, Z., DAI, X., ZHOU, Y., LI, Y., CAO, X. (2015). The assembly of virus-like particles of porcine transmissible gastroenteritisvirus in vitro by baculovirus expression system. Turkish Journal of Veterinary and Animal Sciences, Cilt: 39 - Sayı: 3, 302. https://ajindex.com/articles/121410

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